Enzymes
| UniProtKB help_outline | 1 proteins |
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Name help_outline
[(2→6)-α-D-glucosyl-(1→4)-N-acetyl-α-D-neuraminosyl]n
Identifier
CHEBI:139287
Charge
-1
Formula
(C17H26NO13)n.H2O
Search links
Involved in 2 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:14318Polymer name: [(2→6)-α-D-glucosyl-(1→4)-N-acetyl-α-D-neuraminosyl](n)Polymerization index help_outline nFormula H2O(C17H26NO13)nCharge (0)(-1)nMol File for the polymer
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- Name help_outline acetyl-CoA Identifier CHEBI:57288 (Beilstein: 8468140) help_outline Charge -4 Formula C23H34N7O17P3S InChIKeyhelp_outline ZSLZBFCDCINBPY-ZSJPKINUSA-J SMILEShelp_outline CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 352 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
[(2→6)-α-D-glucosyl-(1→4)-N,O9-diacetyl-α-D-neuraminosyl]n
Identifier
CHEBI:139289
Charge
-1
Formula
(C19H28NO14)n.H2O
Search links
Involved in 1 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:14320Polymer name: [(2→6)-α-D-glucosyl-(1→4)-N,O9-diacetyl-α-D-neuraminosyl](n)Polymerization index help_outline nFormula H2O(C19H28NO14)nCharge (0)(-1)nMol File for the polymer
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- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,500 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:55852 | RHEA:55853 | RHEA:55854 | RHEA:55855 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Structural and kinetic characterizations of the polysialic acid O-acetyltransferase OatWY from Neisseria meningitidis.
Lee H.J., Rakic B., Gilbert M., Wakarchuk W.W., Withers S.G., Strynadka N.C.
The neuroinvasive pathogen Neisseria meningitidis has 13 capsular serogroups, but the majority of disease is caused by only 5 of these. Groups B, C, Y, and W-135 all display a polymeric sialic acid-containing capsule that provides a means for the bacteria to evade the immune response during infect ... >> More
The neuroinvasive pathogen Neisseria meningitidis has 13 capsular serogroups, but the majority of disease is caused by only 5 of these. Groups B, C, Y, and W-135 all display a polymeric sialic acid-containing capsule that provides a means for the bacteria to evade the immune response during infection by mimicking host sialic acid-containing cell surface structures. These capsules in serogroups C, Y, and W-135 can be further acetylated by a sialic acid-specific O-acetyltransferase, a modification that correlates with decreased immunoreactivity and increased virulence. In N. meningitidis serogroup Y, the O-acetylation reaction is catalyzed by the enzyme OatWY, which we show has clear specificity toward the serogroup Y capsule ([Glc-(alpha1-->4)-Sia](n)). To understand the underlying molecular basis of this process, we have performed crystallographic analysis of OatWY with bound substrate as well as determined kinetic parameters of the wild type enzyme and active site mutants. The structure of OatWY reveals an intimate homotrimer of left-handed beta-helix motifs that frame a deep active site cleft selective for the polysialic acid-bearing substrate. Within the active site, our structural, kinetic, and mutagenesis data support the role of two conserved residues in the catalytic mechanism (His-121 and Trp-145) and further highlight a significant movement of Tyr-171 that blocks the active site of the enzyme in its native form. Collectively, our results reveal the first structural features of a bacterial sialic acid O-acetyltransferase and provide significant new insight into its catalytic mechanism and specificity for the capsular polysaccharide of serogroup Y meningococci. << Less
J. Biol. Chem. 284:24501-24511(2009) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.